Recombinant Human HSP27 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications InhibAct
Format
Carrier-Free

Order Details

Recombinant Human HSP27 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit apoptosis in human neutrophils. Sheth, K. et al. (2001) J. Surg. Res. 99:129. 1 μg/mL of Recombinant Human HSP27 will reduce neutrophil apoptosis by more than 25%.
Optimal dilutions should be determined by each laboratory for each application.
Source
E. coli-derived
Thr2-Lys205, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Thr2
Protein/Peptide Type
Recombinant Proteins
Gene
HSPB1
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
23.6 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
28 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in HEPES, NaCl and DTT.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human HSP27 Protein, CF

  • 28 kDa heat shock protein
  • DKFZp586P1322
  • Estrogen-regulated 24 kDa protein
  • Heat shock 27 kDa protein
  • heat shock 27kD protein 1
  • heat shock 27kDa protein 1
  • heat shock protein beta-1
  • HMN2B
  • HS.76067
  • HSP25
  • HSP27
  • HSP27HSP 27
  • HSP28CMT2F
  • HSPB1
  • SRP27
  • Stress-responsive protein 27

Background

Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up-regulated in response to cellular stress. Elevated levels of HSPs have been observed in association with ischemia/reperfusion, cancer, and chronic heart failure. HSP27 is a member of the small heat shock protein family, which also includes HSP25 and the alpha -crystallins. HSP27 forms a large oligomer and the extent of phosphorylation plays a role in determining specific functions. HSP27 also functions as an anti-apoptotic molecule, regulating apoptosis through direct interaction with key components of the apoptotic pathway. HSP27 binds and sequesters cytochrome c released from the mitochondria in response to an apoptotic stimulus. This prevents the proper assembly of the apoptosome and subsequently, the activation of procaspase-9 and procaspase-3.

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Bioinformatics

Gene Symbol HSPB1
Entrez
Uniprot